Characterization of Cytochrome P450 Enzymes and Their Applications in Synthetic Biology.

Autor: Jeffreys LN; Manchester Institute of Biotechnology, University of Manchester, Manchester, United Kingdom., Girvan HM; Manchester Institute of Biotechnology, University of Manchester, Manchester, United Kingdom., McLean KJ; Manchester Institute of Biotechnology, University of Manchester, Manchester, United Kingdom., Munro AW; Manchester Institute of Biotechnology, University of Manchester, Manchester, United Kingdom. Electronic address: andrew.munro@manchester.ac.uk.
Jazyk: angličtina
Zdroj: Methods in enzymology [Methods Enzymol] 2018; Vol. 608, pp. 189-261. Date of Electronic Publication: 2018 Aug 20.
DOI: 10.1016/bs.mie.2018.06.013
Abstrakt: The cytochrome P450 monooxygenase enzymes (P450s) catalyze a diverse array of chemical transformations, most originating from the insertion of an oxygen atom into a substrate that binds close to the P450 heme. The oxygen is delivered by a highly reactive heme iron-oxo species (compound I) and, according to the chemical nature of the substrate and its position in the active site, the P450 can catalyze a wide range of reactions including, e.g., hydroxylation, reduction, decarboxylation, sulfoxidation, N- and O-demethylation, epoxidation, deamination, CC bond formation and breakage, nitration, and dehalogenation. In this chapter, we describe the structural, biochemical, and catalytic properties of the P450s, along with spectroscopic and analytical methods used to characterize P450 enzymes and their redox partners. Important uses of P450 enzymes are highlighted, including how various P450s have been exploited for applications in synthetic biology.
(© 2018 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE